UniProt O41094
Histone H3 Lysine Methyltransferase (O41094)
Histone H3 Lysine Methyltransferase (UniProt O41094): 8 experimental structures on GenesisL1, 4 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- O41094
- Protein
- Histone H3 Lysine Methyltransferase
- Experimental structures
- 8
- Predicted models
- 0
- Pockets
- 4 · 0 records with a druggable one
Structures
8 records of O41094 in the MolNFT archive: 8 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 1N3J | Structure and Substrate of a Histone H3 Lysine Methyltransferase from Paramecium Bursaria Chlorella… | solution nmr | A, B | — | 4 (best 0.49) |
| 1N3J | Structure and substrate of a histone H3 lysine methyltransferase from paramecium bursaria chlorella… | solution nmr | A, B | — | — |
| 3KMA | Crystal Structure of vSET under Condition A | x-ray diffraction | A, B | — | — |
| 3KMA | Crystal structure of vset under condition a | x-ray diffraction | A, B | — | — |
| 3KMJ | Crystal structure of vSET under condition B | x-ray diffraction | A | — | — |
| 3KMJ | Crystal structure of vset under condition B | x-ray diffraction | A | — | — |
| 3KMT | Crystal structure of vSET/SAH/H3 ternary complex | x-ray diffraction | A, B, C | — | — |
| 3KMT | Crystal structure of VSET/SAH/H3 ternary complex | x-ray diffraction | A, B, C | — | — |
Elsewhere
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